InterPro : IPR020693

Name  Tyrosine-protein kinase, non-receptor Jak2 Short Name  Tyr_kinase_non-rcpt_Jak2
Type  Family Description  Janus kinases (JAKs) are tyrosine kinases that function in membrane-proximal signalling events initiated by a variety of extracellular factors binding to cell surface receptors []. Many type I and II cytokine receptors lack a protein tyrosine kinase domain and rely on JAKs to initiate the cytoplasmic signal transduction cascade. Ligand binding induces oligomerisation of the receptors, which then activates the cytoplasmic receptor-associated JAKs. These subsequently phosphorylate tyrosine residues along the receptor chains with which they are associated. The phosphotyrosine residues are a target for a variety of SH2 domain-containing transducer proteins. Amongst these are the signal transducers and activators of transcription (STAT) proteins, which, after binding to the receptor chains, are phosphorylated by the JAK proteins. Phosphorylation enables the STAT proteins to dimerise and translocate into the nucleus, where they alter the expression of cytokine-regulated genes. This system is knownas the JAK-STAT pathway.Four mammalian JAK family members have been identified: JAK1, JAK2, JAK3, and TYK2. They are relatively large kinases of approximately 1150 amino acids, with molecular weights of ~120-130kDa. Their amino acid sequences are characterised by the presence of 7 highly conserved domains, termed JAK homology (JH) domains. The C-terminal domain (JH1) is responsible for the tyrosine kinase function. The next domain in the sequence (JH2) is known as the tyrosine kinase-like domain, as its sequence shows high similarity to functional kinases but does not possess any catalytic activity. Although the function of this domain is not well established, there is some evidence for a regulatory role on the JH1 domain, thus modulating catalytic activity. The N-terminal portion of the JAKs (spanning JH7 to JH3) is important for receptor association and non-catalytic activity.This entry represents the non-receptor tyrosine kinase JAK2 []. JAK2 was initially cloned using a PCR-based strategy utilising primers corresponding to conserved motifs within the catalytic domain of protein-tyrosine kinases []. In common with JAK1 and TYK2, and by contrast with JAK3, JAK2 appears to be ubiquitously expressed.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

9 Contains

Id Name Short Name Type
IPR011009 Protein kinase-like domain Kinase-like_dom Domain
IPR000719 Protein kinase domain Prot_kinase_dom Domain
IPR001245 Serine-threonine/tyrosine-protein kinase catalytic domain Ser-Thr/Tyr_kinase_cat_dom Domain
IPR000980 SH2 domain SH2 Domain
IPR017441 Protein kinase, ATP binding site Protein_kinase_ATP_BS Binding_site
IPR000299 FERM domain FERM_domain Domain
IPR019749 Band 4.1 domain Band_41_domain Domain
IPR020635 Tyrosine-protein kinase, catalytic domain Tyr_kinase_cat_dom Domain
IPR008266 Tyrosine-protein kinase, active site Tyr_kinase_AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR016251 Tyrosine-protein kinase, non-receptor Jak/Tyk2 Tyr_kinase_non-rcpt_Jak/Tyk2 Family

2 Publications

First Author Title Year Journal Volume Pages
Ghoreschi K Janus kinases in immune cell signaling. 2009 Immunol Rev 228 273-87
Wilks AF Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. 1991 Mol Cell Biol 11 2057-65



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)